EUTP_SALTY
ID EUTP_SALTY Reviewed; 159 AA.
AC P0A208; Q9ZFV6;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Probable acetate kinase EutP {ECO:0000303|PubMed:26448059};
DE EC=2.7.2.1 {ECO:0000269|PubMed:26448059};
DE AltName: Full=Ethanolamine utilization protein EutP;
GN Name=eutP; OrderedLocusNames=STM2469;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=10464203; DOI=10.1128/jb.181.17.5317-5329.1999;
RA Kofoid E.C., Rappleye C.A., Stojiljkovic I., Roth J.R.;
RT "The 17-gene ethanolamine (eut) operon of Salmonella typhimurium encodes
RT five homologues of carboxysome shell proteins.";
RL J. Bacteriol. 181:5317-5329(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP FUNCTION, PATHWAY, OPERON, AND INDUCTION BY ETHANOLAMINE AND COBALAMIN.
RC STRAIN=LT2;
RX PubMed=3045078; DOI=10.1128/jb.170.9.3855-3863.1988;
RA Roof D.M., Roth J.R.;
RT "Ethanolamine utilization in Salmonella typhimurium.";
RL J. Bacteriol. 170:3855-3863(1988).
RN [4]
RP DISRUPTION PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=16585748; DOI=10.1128/jb.188.8.2865-2874.2006;
RA Penrod J.T., Roth J.R.;
RT "Conserving a volatile metabolite: a role for carboxysome-like organelles
RT in Salmonella enterica.";
RL J. Bacteriol. 188:2865-2874(2006).
RN [5]
RP POSSIBLE FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, NO COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=26448059; DOI=10.1111/mmi.13243;
RA Moore T.C., Escalante-Semerena J.C.;
RT "The EutQ and EutP proteins are novel acetate kinases involved in
RT ethanolamine catabolism: physiological implications for the function of the
RT ethanolamine metabolosome in Salmonella enterica.";
RL Mol. Microbiol. 99:497-511(2016).
RN [6]
RP FUNCTION.
RC STRAIN=LT2;
RX PubMed=27063436; DOI=10.1038/srep24359;
RA Held M., Kolb A., Perdue S., Hsu S.Y., Bloch S.E., Quin M.B.,
RA Schmidt-Dannert C.;
RT "Engineering formation of multiple recombinant Eut protein nanocompartments
RT in E. coli.";
RL Sci. Rep. 6:24359-24359(2016).
RN [7]
RP FUNCTION.
RC STRAIN=SL1344;
RX PubMed=29531136; DOI=10.1128/iai.00172-18;
RA Anderson C.J., Satkovich J., Koeseoglu V.K., Agaisse H., Kendall M.M.;
RT "The Ethanolamine Permease EutH Promotes Vacuole Adaptation of Salmonella
RT enterica and Listeria monocytogenes during Macrophage Infection.";
RL Infect. Immun. 86:0-0(2018).
CC -!- FUNCTION: A putative bidirectional acetate kinase that may drive flux
CC through the ethanolamine (EA) degradation pathway under anoxic
CC conditions found when this bacteria infects host intestine. It may
CC generate ATP that can be used by other enzymes (EutA and EutT) in the
CC eut pathway. Can use GTP instead of ATP with reduced efficiency
CC (PubMed:26448059). Overexpression in E.coli yields elongated protein
CC sheets; prevents artificial BMC formation by eutS alone or by eutK,
CC eutL, eutM, eutN, eutS in E.coli (PubMed:27063436).
CC {ECO:0000269|PubMed:26448059, ECO:0000269|PubMed:27063436}.
CC -!- FUNCTION: Expression of the eut operon allows this bacteria to use
CC ethanolamine (EA) as a carbon, nitrogen and energy source. It relies on
CC cobalamin (vitamin B12) both as a cofactor for the ethanolamine
CC ammonia-lyase (EAL) activity and to induce the operon (PubMed:3045078).
CC EA enhances bacterial survival in macrophages in a concentration-
CC dependent manner, suggesting it is an important nutrient during
CC infection (PubMed:29531136). {ECO:0000269|PubMed:29531136,
CC ECO:0000269|PubMed:3045078}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetate + ATP = acetyl phosphate + ADP; Xref=Rhea:RHEA:11352,
CC ChEBI:CHEBI:22191, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:456216; EC=2.7.2.1;
CC Evidence={ECO:0000269|PubMed:26448059};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11353;
CC Evidence={ECO:0000269|PubMed:26448059};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11354;
CC Evidence={ECO:0000269|PubMed:26448059};
CC -!- COFACTOR:
CC Note=Does not need divalent cations. {ECO:0000269|PubMed:26448059};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.7 mM for acetate {ECO:0000269|PubMed:26448059};
CC KM=0.5 mM for ATP {ECO:0000269|PubMed:26448059};
CC Note=kcat is 545 sec(-1). {ECO:0000269|PubMed:26448059};
CC -!- PATHWAY: Amine and polyamine degradation; ethanolamine degradation.
CC {ECO:0000269|PubMed:3045078}.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC {ECO:0000305|PubMed:26448059}.
CC -!- INDUCTION: Part of the 17-gene eut operon transcribed from a single
CC promoter, induced by ethanolamine and adenosylcobalamin (AdoCbl,
CC vitamin B12). {ECO:0000269|PubMed:3045078}.
CC -!- DISRUPTION PHENOTYPE: Not required for aerobic growth on ethanolamine
CC (EA) supplemented with cobalamin (vitamin B12). A quadruple eutP-eutQ-
CC eutT-eutD deletion is also not required for growth in the above
CC conditions (PubMed:10464203). A non-polar deletion mutant grows on EA
CC from pH 5.5 to pH 8.0, but does not grow at pH 8.5, releases slightly
CC increased amounts of acetaldehyde on EA plus vitamin B12
CC (PubMed:16585748). No visible phenotype when grown on EA and
CC tetrathionate under anoxic conditions (PubMed:26448059).
CC {ECO:0000269|PubMed:10464203, ECO:0000269|PubMed:16585748,
CC ECO:0000269|PubMed:26448059}.
CC -!- SIMILARITY: Belongs to the EutP/PduV family. {ECO:0000305}.
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DR EMBL; AF093749; AAC78112.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21363.1; -; Genomic_DNA.
DR RefSeq; NP_461404.1; NC_003197.2.
DR RefSeq; WP_000820751.1; NC_003197.2.
DR AlphaFoldDB; P0A208; -.
DR STRING; 99287.STM2469; -.
DR PaxDb; P0A208; -.
DR EnsemblBacteria; AAL21363; AAL21363; STM2469.
DR GeneID; 1253991; -.
DR KEGG; stm:STM2469; -.
DR PATRIC; fig|99287.12.peg.2607; -.
DR HOGENOM; CLU_113298_2_0_6; -.
DR OMA; PGEYMEN; -.
DR PhylomeDB; P0A208; -.
DR BioCyc; MetaCyc:STM2469-MON; -.
DR BioCyc; SENT99287:STM2469-MON; -.
DR UniPathway; UPA00560; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0031469; C:bacterial microcompartment; IEA:UniProtKB-SubCell.
DR GO; GO:0008776; F:acetate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046336; P:ethanolamine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR012381; EutP_PduV.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR40453; PTHR40453; 1.
DR Pfam; PF10662; PduV-EutP; 1.
DR PIRSF; PIRSF036409; EutP_PduV; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02528; EutP; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Bacterial microcompartment; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase; Virulence.
FT CHAIN 1..159
FT /note="Probable acetate kinase EutP"
FT /id="PRO_0000087096"
FT BINDING 8..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 159 AA; 17726 MW; C674D376409FAA83 CRC64;
MKRIAFVGAV GAGKTTLFNA LRGNYSLARK TQAVEFNDHG DIDTPGEYFS HPRWYHALIT
TLQDVDTLIY VHAANDKESR LPAGLLDVGT RKRHIAVISK TDMPDADVAA TRQLLCEIGF
REPIFELNGH DPQSVRQLVD YLAALSEQEE EAGEKTYHS
